Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins (Q30176641)

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English	Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

9 June 2017

Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins (English)

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Europe PubMed Central

PubMed publication ID

9 June 2017

protein folding

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author name string

Zhang O

1

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PubMed publication ID

9 June 2017

Forman-Kay JD

2

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PubMed publication ID

9 June 2017

Shortle D

3

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9 June 2017

Kay LE

4

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9 June 2017

language of work or name

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publication date

1 February 1997

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9 June 2017

Journal of Biomolecular NMR

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9 June 2017

9

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PubMed publication ID

9 June 2017

2

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PubMed publication ID

9 June 2017

181-200

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PubMed publication ID

9 June 2017

A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding

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12 December 2020

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Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.

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https://pubmed.ncbi.nlm.nih.gov/9090132

12 December 2020

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Protein modules and signalling networks

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https://pubmed.ncbi.nlm.nih.gov/9090132

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques

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https://pubmed.ncbi.nlm.nih.gov/9090132

12 December 2020

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Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.

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https://pubmed.ncbi.nlm.nih.gov/9090132

12 December 2020

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Coupling of local folding to site-specific binding of proteins to DNA

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A novel viral oncogene with structural similarity to phospholipase C

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Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution.

1 reference

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Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin

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The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A

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DNA recognition by proteins with the helix-turn-helix motif

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A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.

1 reference

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12 December 2020

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Solid state NMR studies of protein internal dynamics

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Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

1 reference

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A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos.

1 reference

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Protein folding in the cell: competing models of chaperonin function.

1 reference

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Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol

1 reference

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The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase

1 reference

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Staphylococcal nuclease: sequential assignments and solution structure

1 reference

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Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy

1 reference

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NMR determination of residual structure in a urea-denatured protein, the 434-repressor

1 reference

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Protein biogenesis: chaperones for nascent polypeptides

1 reference

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Structural analysis of non-native states of proteins by NMR methods

1 reference

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Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state

1 reference

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An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro

1 reference

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Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride

1 reference

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Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution

1 reference

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NMR strategy for determining Xaa-Pro peptide bond configurations in proteins: mutants of staphylococcal nuclease with altered configuration at proline-117

1 reference

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12 December 2020

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Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9090132

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1023/A:1018658305040

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Europe PubMed Central

PubMed publication ID

9 June 2017

Dimensions Publication ID

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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